Improvement of antibody immobilization using hyperbranched polymer and protein A

2011 ◽  
Vol 409 (1) ◽  
pp. 22-27 ◽  
Author(s):  
Guangyu Shen ◽  
Chenbo Cai ◽  
Kun Wang ◽  
Jilin Lu
Keyword(s):  
Hyperbranched Polymer ◽  
Protein A ◽  
Antibody Immobilization

Effectiveness of protein A for antibody immobilization for a fiber optic biosensor

1997 ◽  
Vol 12 (4) ◽  
pp. 329-336 ◽  
Author(s):  
George P. Anderson ◽  
Meagan A. Jacoby ◽  
Frances S. Ligler ◽  
Keeley D. King
Keyword(s):  
Fiber Optic ◽  
Protein A ◽  
Antibody Immobilization

scholarly journals Comparative Assessment of Affinity-Based Techniques for Oriented Antibody Immobilization towards Immunosensor Performance Optimization

2019 ◽  
Vol 2019 ◽  
pp. 1-10 ◽  
Author(s):  
George Tsekenis ◽  
Marianneza Chatzipetrou ◽  
Maria Massaouti ◽  
Ioanna Zergioti
Keyword(s):  
Performance Optimization ◽  
Surface Density ◽  
Critical Role ◽  
Protein A ◽  
Antigen Binding ◽  
Antibody Immobilization ◽  
Functionalized Surfaces ◽  
Antigen System ◽  
Complex Engineering ◽  
First Time

Immunosensor sensitivity and stability depend on a number of parameters such as the orientation, the surface density, and the antigen-binding efficiency of antibodies following their immobilization onto functionalized surfaces. A number of techniques have been developed to improve the performance of an immunosensor that targets one or both of the parameters mentioned above. Herein, two widely employed techniques are compared for the first time, which do not require any complex engineering of neither the antibodies nor the surfaces onto which the former get immobilized. To optimize the different surface functionalization protocols and compare their efficiency, a model antibody-antigen system was employed that resembles the complex matrices immunosensors are frequently faced with in real conditions. The obtained results reveal that protein A/G is much more efficient in increasing antibody loading onto the surfaces in comparison to boronate ester chemistry. Despite the fact, therefore, that both contribute towards the orientation-specific immobilization of antibodies and hence enhance their antigen-binding efficiency, it is the increased antibody surface density attained with the use of protein A/G that plays a critical role in achieving maximal antigen recognition.

scholarly journals Use of Immunomatrix Methods to Improve Protein-Protein Interaction Detection

2003 ◽  
Vol 2003 (5) ◽  
pp. 291-298 ◽  
Author(s):  
M. Walid Qoronfleh ◽  
Ling Ren ◽  
Daryl Emery ◽  
Maria Perr ◽  
Barbara Kaboord
Keyword(s):  
Protein Interactions ◽  
Protein A ◽  
Light Chains ◽  
Protein G ◽  
Antibody Immobilization ◽  
Protein Protein Interactions ◽  
Protein Protein Interaction ◽  
Interaction Detection ◽  
Main Disadvantage ◽  
Key Techniques

Immunoprecipitation (IP) and coimmunoprecipitation (co-IP) are key techniques for studying protein-protein interactions. These methods utilize immobilized protein A or protein G to isolate antibody-bound target antigens. The main disadvantage of traditional immunoprecipitation and coimmunoprecipitation is that the conditions used to elute the precipitated antigen also release the antibody, contaminating the antigen and destroying the antibody support. To overcome these problems, we describe two methods to generate a reusable antibody support by cross-linking the antibody to immobilized protein A or protein G, or by coupling it directly to the resin. Our studies have demonstrated that the immobilization efficiency for the antibody coupling method was similar for several species of antibody. Furthermore, we illustrate that using both methods of antibody immobilization yields IP and co-IP results similar to traditional protocols but eliminate the antibody heavy and light chains contamination.

Site-directed antibody immobilization using a protein A–gold binding domain fusion protein for enhanced SPR immunosensing

The Analyst ◽  
2013 ◽  
Vol 138 (7) ◽  
pp. 2023 ◽  
Author(s):  
Elena de Juan-Franco ◽  
Antonio Caruz ◽  
J. R. Pedrajas ◽  
Laura M. Lechuga
Keyword(s):  
Fusion Protein ◽  
Protein A ◽  
Binding Domain ◽  
Antibody Immobilization ◽  
Domain Fusion

Protein A Langmuir-Blodgett Film for Antibody Immobilization and Its Use in Optical Immunosensing

1995 ◽  
Vol 67 (9) ◽  
pp. 1613-1616 ◽  
Author(s):  
Koji. Owaku ◽  
Masahiro. Goto ◽  
Yoshihito. Ikariyama ◽  
Masuo. Aizawa
Keyword(s):  
Protein A ◽  
Antibody Immobilization ◽  
Blodgett Film ◽  
Langmuir Blodgett ◽  
Langmuir Blodgett Film

Use of Protein a Conjugated to Peroxidase to Localize Immunoglobulin G in SSPE Ferret Brain

1982 ◽  
Vol 40 ◽  
pp. 350-351
Author(s):  
Hannah R. Brown ◽  
Anthony F. Nostro ◽  
Halldor Thormar
Keyword(s):  
Immunoglobulin G ◽  
Human Disease ◽  
Measles Virus ◽  
Subacute Sclerosing Panencephalitis ◽  
Protein A ◽  
Inflammatory Lesions ◽  
Sspe Virus ◽  
Specific Immunoglobulin ◽  
Antibody Titers ◽  
The Brain

Subacute sclerosing panencephalitis (SSPE) is a slowly progressing disease of the CNS in children which is caused by measles virus. Ferrets immunized with measles virus prior to inoculation with the cell associated, syncytiogenic D.R. strain of SSPE virus exhibit characteristics very similar to the human disease. Measles virus nucleocapsids are present, high measles antibody titers are found in the sera and inflammatory lesions are prominent in the brains. Measles virus specific immunoglobulin G (IgG) is present in the brain,and IgG/ albumin ratios indicate that the antibodies are synthesized within the CNS.

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